2EHB
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-02-16 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.137, 57.387, 141.896 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 70.890 - 2.100 |
| R-factor | 0.2168 |
| Rwork | 0.215 |
| R-free | 0.25932 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Structure of SOS3 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.388 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.900 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.060 | 0.350 |
| Number of reflections | 25141 | |
| <I/σ(I)> | 9.7 | 2.6 |
| Completeness [%] | 99.3 | 92.7 |
| Redundancy | 4.4 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | drops: 10mg/ml SOS3:C-SOS2, reservoir solution: 20%(w/v) PEG4000, 0.1M Tris-HCl pH 7.5, 0.2M Lithium Sulfate, 3%(v/v) Ethylene Glycol; 1M Guanidine HCl in a ratio of 1:1:0.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
